RGCC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RGCC_HUMAN
• UniProt AC: Q9H4X1
• Protein Name: Regulator of cell cycle RGCC
• Gene Name: RGCC
• Organism: Homo sapiens (Human).
• Sequence Length: 137
• Subcellular Localization: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase.
• Protein Description: Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation..
• Protein Sequence: MKPPAAQGSPAAAAAAAPALDSAAAEDLSDALCEFDAVLADFASPFHERHFHYEEHLERMKRRSSASVSDSSGFSDSESADSLYRNSFSFSDEKLNSPTDSTPALLSATVTPQKAKLGDTKELEAFIADLDKTLASM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	KPPAAQGSPAAAAAA CCCHHHCCHHHHHHH	10.17	26074081
29	Phosphorylation	SAAAEDLSDALCEFD HHHHHHHHHHHHHHH	32.91	22817900
44	Phosphorylation	AVLADFASPFHERHF HHHHHHCCCHHHHHC	28.26	26074081
53	Phosphorylation	FHERHFHYEEHLERM HHHHHCCHHHHHHHH	23.28	28796482
64	Phosphorylation	LERMKRRSSASVSDS HHHHHHHHCCCCCCC	34.00	30242111
65	Phosphorylation	ERMKRRSSASVSDSS HHHHHHHCCCCCCCC	23.81	21712546
67	Phosphorylation	MKRRSSASVSDSSGF HHHHHCCCCCCCCCC	24.89	30242111
69	Phosphorylation	RRSSASVSDSSGFSD HHHCCCCCCCCCCCC	29.31	21082442
71	Phosphorylation	SSASVSDSSGFSDSE HCCCCCCCCCCCCCH	25.51	21082442
72	Phosphorylation	SASVSDSSGFSDSES CCCCCCCCCCCCCHH	49.17	28122231
75	Phosphorylation	VSDSSGFSDSESADS CCCCCCCCCCHHHHH	43.69	21082442
77	Phosphorylation	DSSGFSDSESADSLY CCCCCCCCHHHHHHH	32.05	30576142
79	Phosphorylation	SGFSDSESADSLYRN CCCCCCHHHHHHHHC	41.13	28060719
82	Phosphorylation	SDSESADSLYRNSFS CCCHHHHHHHHCCCC	27.32	28060719
84	Phosphorylation	SESADSLYRNSFSFS CHHHHHHHHCCCCCC	16.23	28060719
87	Phosphorylation	ADSLYRNSFSFSDEK HHHHHHCCCCCCCHH	17.17	26657352
89	Phosphorylation	SLYRNSFSFSDEKLN HHHHCCCCCCCHHCC	24.54	21712546
91	Phosphorylation	YRNSFSFSDEKLNSP HHCCCCCCCHHCCCC	43.60	21712546
97	Phosphorylation	FSDEKLNSPTDSTPA CCCHHCCCCCCCCCC	39.34	28355574
99	Phosphorylation	DEKLNSPTDSTPALL CHHCCCCCCCCCCHH	42.26	30175587
101	Phosphorylation	KLNSPTDSTPALLSA HCCCCCCCCCCHHHH	38.48	28787133
102	Phosphorylation	LNSPTDSTPALLSAT CCCCCCCCCCHHHHE	18.52	28787133
107	Phosphorylation	DSTPALLSATVTPQK CCCCCHHHHEECCCC	23.81	22617229
109	Phosphorylation	TPALLSATVTPQKAK CCCHHHHEECCCCCC	22.87	21712546
111	Phosphorylation	ALLSATVTPQKAKLG CHHHHEECCCCCCCC	18.69	30175587
133	Phosphorylation	FIADLDKTLASM--- HHHHHHHHHHCC---	27.50	21712546
136	Phosphorylation	DLDKTLASM------ HHHHHHHCC------	28.30	21712546

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
111	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RGCC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RGCC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK1_HUMAN	CDK1	physical	11687586
AKT1_HUMAN	AKT1	physical	19162005
TLN2_HUMAN	TLN2	physical	26186194
TLN1_HUMAN	TLN1	physical	26186194
TRAF7_HUMAN	TRAF7	physical	26186194
SYCM_HUMAN	CARS2	physical	26186194
PLK1_HUMAN	PLK1	physical	17146433
TLN2_HUMAN	TLN2	physical	28514442
SYCM_HUMAN	CARS2	physical	28514442
TLN1_HUMAN	TLN1	physical	28514442
TRAF7_HUMAN	TRAF7	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-75;SER-97 AND THR-111, AND MASS SPECTROMETRY.
PubMed: 19690332

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-29 AND SER-44,AND MASS SPECTROMETRY.
PubMed: 17081983

"RGC-32 increases p34CDC2 kinase activity and entry of aortic smoothmuscle cells into S-phase.";
Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V.,Shin M.L., Rus H.;
J. Biol. Chem. 277:502-508(2002).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION,SUBCELLULAR LOCATION, MUTAGENESIS OF THR-111, PHOSPHORYLATION ATTHR-111, AND TISSUE SPECIFICITY.
PubMed: 11687586